PUR7_YEAST - dbPTM
PUR7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUR7_YEAST
UniProt AC P27616
Protein Name Phosphoribosylaminoimidazole-succinocarboxamide synthase
Gene Name ADE1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 306
Subcellular Localization
Protein Description
Protein Sequence MSITKTELDGILPLVARGKVRDIYEVDAGTLLFVATDRISAYDVIMENSIPEKGILLTKLSEFWFKFLSNDVRNHLVDIAPGKTIFDYLPAKLSEPKYKTQLEDRSLLVHKHKLIPLEVIVRGYITGSAWKEYVKTGTVHGLKQPQGLKESQEFPEPIFTPSTKAEQGEHDENISPAQAAELVGEDLSRRVAELAVKLYSKCKDYAKEKGIIIADTKFEFGIDEKTNEIILVDEVLTPDSSRFWNGASYKVGESQDSYDKQFLRDWLTANKLNGVNGVKMPQDIVDRTRAKYIEAYETLTGSKWSH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MSITKTEL
-------CCCCHHHH		6.20-
2Acetylation------MSITKTELD
------CCCCHHHHC		38.689551557
6Phosphorylation--MSITKTELDGILP
--CCCCHHHHCCCHH		32.8822369663
53UbiquitinationMENSIPEKGILLTKL
HHCCCCCCCEEHHHH		45.9924961812
83AcetylationLVDIAPGKTIFDYLP
CCCCCCCCCHHHHCC		37.0724489116
92AcetylationIFDYLPAKLSEPKYK
HHHHCCCCCCCCCHH		51.0824489116
1112-HydroxyisobutyrylationDRSLLVHKHKLIPLE
CCCEEEECCCCCCHH		34.65-
113AcetylationSLLVHKHKLIPLEVI
CEEEECCCCCCHHHH		53.5724489116
126PhosphorylationVIVRGYITGSAWKEY
HHHCCEECCHHHHHH		19.3222369663
128PhosphorylationVRGYITGSAWKEYVK
HCCEECCHHHHHHHH		23.4722369663
131AcetylationYITGSAWKEYVKTGT
EECCHHHHHHHHHCC		38.5924489116
136PhosphorylationAWKEYVKTGTVHGLK
HHHHHHHHCCCCCCC		28.2128889911
138PhosphorylationKEYVKTGTVHGLKQP
HHHHHHCCCCCCCCC		17.9828889911
160PhosphorylationEFPEPIFTPSTKAEQ
CCCCCCCCCCCCCCC		19.6328889911
2092-HydroxyisobutyrylationCKDYAKEKGIIIADT
CHHHHHHCCEEEEEC		55.49-
209AcetylationCKDYAKEKGIIIADT
CHHHHHHCCEEEEEC		55.4925381059
257PhosphorylationKVGESQDSYDKQFLR
ECCCCCCCCCHHHHH		27.8228889911
258PhosphorylationVGESQDSYDKQFLRD
CCCCCCCCCHHHHHH		35.1328889911
260UbiquitinationESQDSYDKQFLRDWL
CCCCCCCHHHHHHHH		34.4123749301
260AcetylationESQDSYDKQFLRDWL
CCCCCCCHHHHHHHH		34.4124489116
291UbiquitinationIVDRTRAKYIEAYET
HHHHHHHHHHHHHHH		43.3923749301
291AcetylationIVDRTRAKYIEAYET
HHHHHHHHHHHHHHH		43.3924489116
303AcetylationYETLTGSKWSH----
HHHHHCCCCCC----		54.8024489116
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PUR7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUR7_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PUR7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP71_YEASTSSA1physical
19536198
HPRT_YEASTHPT1genetic
21623372
FCY2_YEASTFCY2genetic
21623372
FUMH_YEASTFUM1genetic
21623372
TNA1_YEASTTNA1genetic
21623372
PUR2_YEASTADE5,7genetic
21623372
IMDH3_YEASTIMD3genetic
21623372
COQ2_YEASTCOQ2genetic
21623372
PUR4_YEASTADE6genetic
21623372
PUR92_YEASTADE17genetic
21623372
QCR7_YEASTQCR7genetic
21623372
FABG_YEASTOAR1genetic
21623372
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUR7_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND MASSSPECTROMETRY.

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